Mutation of conserved residues in the laminarinase Lam1092 increases the antioxidant activity of the laminarin product hydrolysates

Li, Jin; Liang, Yumei; He, Zhixiao; Zhong, Min; Hu, Zhong Jie

doi:10.1016/j.enzmictec.2022.110135

Cited by 4 publications

(2 citation statements)

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“…The investigation resulted in establishing eight Lam1092 mutants, and the hydrolysates produced by two of these mutants (G361A and H466A) displayed signicantly improved antioxidant characteristics. 88 The elucidation of the properties and catalytic mechanisms of Lam1092, as described in this research, holds the potential to serve as a benecial reference for identifying novel laminarinases.…”

Section: Wound Healingmentioning

confidence: 95%

From algae to advancements: laminarin in biomedicine

Pramanik,

Singh,

Abualsoud

et al. 2024

RSC Adv.

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Section: Wound Healingmentioning

confidence: 95%

From algae to advancements: laminarin in biomedicine

Pramanik,

Singh,

Abualsoud

et al. 2024

RSC Adv.

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“…family 16 glycosylhydrolase (Figure 5). The enzyme β-1,3-glucanase, especially endo-β-1,3-glucanase, is part of the GH 16 family protein (Mouyna et al 2013;Li et al 2023). Several studies have reported that this enzyme can be produced by several bacteria from the Streptomyces group, such as S. corchorusii UCR3-16 (Tamreihao et al 2016), S. philanthi RM-1-1-38 (Boukaew et al 2016), S. goshikiensis YCXU (Faheem et al 2015), S. violaceusniger MTCC 3959 (Nagpure et al 2014), and S. hygroscopicus subs.…”

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confidence: 99%

Glucanase activity produced by rhizospheric Streptomyces tritolerans ARJ 32 and Streptomyces collinus ARJ 38 and the analysis of their encoding genes

BUDIMAN,

PURWANINGTYAS,

PRIYANTO

et al. 2023

Biodiversitas

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Abstract. Budiman DZ, Purwaningtyas WE, Priyanto JA, Putra IP, Nawangsih AA, Wahyudi AT. 2023. Glucanase activity produced by rhizospheric Streptomyces tritolerans ARJ 32 and Streptomyces collinus ARJ 38 and the analysis of their encoding genes. Biodiversitas 24: 5831-5837. The enzyme ?-1,3-glucanase is capable of breaking down the glucan components in the cell walls of phytopathogenic fungi. Streptomyces spp. isolated from the maize rhizosphere, are believed to produce enzymes with glucanolytic activity, making them promising candidates for use as a biological control agent against these fungi. This work aims to quantitatively analyze the enzymatic activity of glucanase in Streptomyces tritolerans ARJ 32 and Streptomyces collinus ARJ 38 and identify their encoding genes (bglS) and the three-dimensional modeling of their protein structures. The dinitrosalicylic acid (DNS) method quantitively assays the glucanase enzyme. The TA-Cloning of the bglS gene was performed using pGEM-T Easy Plasmid Vector, and the three-dimensional protein structure was constructed using the I-TASSER program. According to the findings, both Streptomyces isolates exhibited glucanolytic activity. The glucanase enzyme activities of S. tritolerans ARJ 32 and S. collinus ARJ 38 peaked at eight days of incubation, with values of 31.116 U/mg and 41.599 U/mg, respectively. The partial bglS gene was present in both Streptomyces and identified as endo-?-1,3-glucanase from the glycoside hydrolase family 16 (GH 16). The deduced partial amino acid sequences were aligned and showed some highly conserved residue in the catalytic domain of GH 16. The three-dimensional structural model built from the partial bglS amino acid sequences displayed high-quality parameters and overlapped with the protein model of partial endo-?-1,3-glucanase from Nocardiopsis sp. F96 (2HYK). These preliminary results suggest that the two Streptomyces isolates had the potential to be used as glucanase enzyme producers.

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